Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/66535
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dc.contributor.authorHao, N.en
dc.contributor.authorWhitelaw, M.L.en
dc.contributor.authorShearwin, K.E.en
dc.contributor.authorDodd, I.B.en
dc.contributor.authorChapman-Smith, A.en
dc.date.issued2011en
dc.identifier.citationNucleic Acids Research, 2011; 39(9):3695-3709en
dc.identifier.issn1362-4962en
dc.identifier.issn0305-1048en
dc.identifier.urihttp://hdl.handle.net/2440/66535-
dc.description.abstractThe basic helix-loop-helix (bHLH).PAS dimeric transcription factors have crucial roles in development, stress response, oxygen homeostasis and neurogenesis. Their target gene specificity depends in part on partner protein choices, where dimerization with common partner Aryl hydrocarbon receptor nuclear translocator (Arnt) is an essential step towards forming active, DNA binding complexes. Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Of these, Arnt E163 and Arnt S190 were selective for the AhR/Arnt interaction, since mutations at these positions had little effect on Arnt dimerization with other bHLH.PAS partners, while substitution of Arnt D217 affected the interaction with both AhR and hypoxia inducible factor-1α but not with single minded 1 and 2 or neuronal PAS4. Arnt uses the same face of the N-terminal PAS domain for homo- and heterodimerization and mutational analysis of AhR demonstrated that the equivalent region is used by AhR when dimerizing with Arnt. These interfaces differ from the PAS β-scaffold surfaces used for dimerization between the C-terminal PAS domains of hypoxia inducible factor-2α and Arnt, commonly used for PAS domain interactions.en
dc.description.statementofresponsibilityNan Hao, Murray L. Whitelaw, Keith E. Shearwin, Ian B. Dodd and Anne Chapman-Smithen
dc.language.isoenen
dc.publisherOxford University Press (OUP)en
dc.rights© The Author(s) 2011. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectCell Line; Animals; Mice; Receptors, Aryl Hydrocarbon; Two-Hybrid System Techniques; Amino Acid Substitution; Evolution, Molecular; Protein Structure, Tertiary; Dimerization; Aryl Hydrocarbon Receptor Nuclear Translocator; Basic Helix-Loop-Helix Transcription Factors; Transcriptional Activationen
dc.titleIdentification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhRen
dc.typeJournal articleen
dc.identifier.rmid0020108738en
dc.identifier.doi10.1093/nar/gkq1336en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP0559011en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP0665185en
dc.identifier.pubid29691-
pubs.library.collectionMolecular and Biomedical Science publicationsen
pubs.library.teamDS04en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Molecular and Biomedical Science publications

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